GeneID: 164



Names

Common Name: GALNT13 Type: Gene
Chromosome: 2 (NC_000002.12) Locus: N/A
HUGO Symbol: GALNT13 Full Name: polypeptide N-acetylgalactosaminyltransferase 13
Exons: 13 Introns: 12

Description:
GALNT13 [UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13 (GalNAc-T13)] is a member of a large family of enzymes (GalNAc-T) that catalyze the O-linked glycosylation of peptides in the Golgi apparatus. Each member has distinct substrate specificity, expression pattern and glycosylation function, indicating that different members regulate distinct cellular processes. These enzymes transfer a single N-acetylgalactosamine (GalNAc) residue to a serine or threonine residue in peptides. Aberrant glycosylation is associated with tumourigenesis and shown to influence different steps in tumor progression, such as proliferation, invasion, metastasis and angiogenesis, which are known to be involved in pulmonary vascular remodelling. Multiple SNPs in this gene were linked to an elevated tricuspid regurgitant jet velocity (TRV) and pulmonary hypertension in sickle cell disease.

Synonyms: GalNAc-T13

Comments:
N/A

Sequence Viewer

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Publications / Origin

  1. Peng C, Togayachi A, Kwon YD, Xie C, Wu G, Zou X, Sato T, Ito H, Tachibana K, Kubota T, Noce T, Narimatsu H, Zhang Y, Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile., Biochem. Biophys. Res. Commun. , 402(4), 680-6, 2010 PubMed
  2. Desai AA, Zhou T, Ahmad H, Zhang W, Mu W, Trevino S, Wade MS, Raghavachari N, Kato GJ, Peters-Lawrence MH, Thiruvoipati T, Turner K, Artz N, Huang Y, Patel AR, Yuan JX, Gordeuk VR, Lang RM, Garcia JG, Machado RF, A novel molecular signature for elevated tricuspid regurgitation velocity in sickle cell disease., Am. J. Respir. Crit. Care Med. , 186(4), 359-68, 2012 PubMed
  3. Schjoldager KT, Joshi HJ, Kong Y, Goth CK, King SL, Wandall HH, Bennett EP, Vakhrushev SY, Clausen H, Deconstruction of O-glycosylation--GalNAc-T isoforms direct distinct subsets of the O-glycoproteome., EMBO Rep. , 16(12), 1713-22, 2015 PubMed
  4. Vasconcelos-Dos-Santos A, Oliveira IA, Lucena MC, Mantuano NR, Whelan SA, Dias WB, Todeschini AR, Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against Cancer., Front Oncol , 5(0), 138, 2015 PubMed
Created on 2016-07-20 15:14:28, Last reviewed on 2016-07-21 09:17:48 (Show full history)


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